ECMDB

Identification

Name:

Bifunctional aspartokinase/homoserine dehydrogenase 1

Synonyms:

Aspartokinase I/homoserine dehydrogenase I
AKI-HDI
Aspartokinase
Homoserine dehydrogenase

Gene Name:

thrA

Enzyme Class:

Biological Properties

General Function:

Involved in amino acid binding

Specific Function:

L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H

Cellular Location:

Not Available

SMPDB Pathways:

Lysine biosynthesis PW000771
Secondary Metabolites: threonine biosynthesis from aspartate PW000976
methionine biosynthesis PW000814
threonine biosynthesis PW000817

KEGG Pathways:

Cysteine and methionine metabolism ec00270
Glycine, serine and threonine metabolism ec00260
Lysine biosynthesis ec00300
Metabolic pathways eco01100
Microbial metabolism in diverse environments ec01120
Monobactam biosynthesis eco00261

KEGG Reactions:

1.0

↔

1.0

1.0L-Aspartic acid + 1.0Adenosine triphosphate ↔ 1.0L-Aspartyl-4-phosphate + 1.0ADP
ReactionCard

1.0

↔

1.0

1.0L-Homoserine + 1.0NADP ↔ 1.0L-Aspartate-semialdehyde + 1.0Hydrogen ion + 1.0NADPH
ReactionCard

1.0

↔

1.0

1.0L-Homoserine + 1.0NAD ↔ 1.0L-Aspartate-semialdehyde + 1.0NADH + 1.0Hydrogen ion
ReactionCard

SMPDB Reactions:

1.0

1.0NADPH

1.0

→

1.0

1.0L-Homoserine

1.0

1.0L-Aspartate-semialdehyde + 1.0Hydrogen ion + 1.0NADPH + 1.0NADPH → 1.0NADP + 1.0L-Homoserine + 1.0L-Homoserine
ReactionCard

EcoCyc Reactions:

1.0

↔

1.0

1.0L-Aspartic acid + 1.0Adenosine triphosphate ↔ 1.0L-Aspartyl-4-phosphate + 1.0ADP
ReactionCard

Complex Reactions:

1.0

1.0NAD(P)(+)

→

1.0

1.0NAD(P)H

1.0L-Homoserine + 1.0NAD(P)(+) → 1.0L-Aspartate-semialdehyde + 1.0NAD(P)H
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB00538	Adenosine triphosphate	MetaboCard
ECMDB01341	ADP	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB12249	L-Aspartate-semialdehyde	MetaboCard
ECMDB00191	L-Aspartic acid	MetaboCard
ECMDB12250	L-Aspartyl-4-phosphate	MetaboCard
ECMDB02251	L-Homoserine	MetaboCard
ECMDB00902	NAD	MetaboCard
ECMDB01487	NADH	MetaboCard
ECMDB00217	NADP	MetaboCard
ECMDB04111	NADPH	MetaboCard

GO Classification:

Function
amino acid binding
aspartate kinase activity
binding
carboxylic acid binding
catalytic activity
homoserine dehydrogenase activity
NADP or NADPH binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
phosphotransferase activity, carboxyl group as acceptor
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
aspartate family amino acid biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid biosynthetic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
oxidation reduction

Gene Properties

Blattner:

b0002

Gene Orientation

Clockwise

Centisome Percentage:

0.01

Left Sequence End

337

Right Sequence End

2799

Gene Sequence:

>2463 bp
ATGCGAGTGTTGAAGTTCGGCGGTACATCAGTGGCAAATGCAGAACGTTTTCTGCGTGTT
GCCGATATTCTGGAAAGCAATGCCAGGCAGGGGCAGGTGGCCACCGTCCTCTCTGCCCCC
GCCAAAATCACCAACCACCTGGTGGCGATGATTGAAAAAACCATTAGCGGCCAGGATGCT
TTACCCAATATCAGCGATGCCGAACGTATTTTTGCCGAACTTTTGACGGGACTCGCCGCC
GCCCAGCCGGGGTTCCCGCTGGCGCAATTGAAAACTTTCGTCGATCAGGAATTTGCCCAA
ATAAAACATGTCCTGCATGGCATTAGTTTGTTGGGGCAGTGCCCGGATAGCATCAACGCT
GCGCTGATTTGCCGTGGCGAGAAAATGTCGATCGCCATTATGGCCGGCGTATTAGAAGCG
CGCGGTCACAACGTTACTGTTATCGATCCGGTCGAAAAACTGCTGGCAGTGGGGCATTAC
CTCGAATCTACCGTCGATATTGCTGAGTCCACCCGCCGTATTGCGGCAAGCCGCATTCCG
GCTGATCACATGGTGCTGATGGCAGGTTTCACCGCCGGTAATGAAAAAGGCGAACTGGTG
GTGCTTGGACGCAACGGTTCCGACTACTCTGCTGCGGTGCTGGCTGCCTGTTTACGCGCC
GATTGTTGCGAGATTTGGACGGACGTTGACGGGGTCTATACCTGCGACCCGCGTCAGGTG
CCCGATGCGAGGTTGTTGAAGTCGATGTCCTACCAGGAAGCGATGGAGCTTTCCTACTTC
GGCGCTAAAGTTCTTCACCCCCGCACCATTACCCCCATCGCCCAGTTCCAGATCCCTTGC
CTGATTAAAAATACCGGAAATCCTCAAGCACCAGGTACGCTCATTGGTGCCAGCCGTGAT
GAAGACGAATTACCGGTCAAGGGCATTTCCAATCTGAATAACATGGCAATGTTCAGCGTT
TCTGGTCCGGGGATGAAAGGGATGGTCGGCATGGCGGCGCGCGTCTTTGCAGCGATGTCA
CGCGCCCGTATTTCCGTGGTGCTGATTACGCAATCATCTTCCGAATACAGCATCAGTTTC
TGCGTTCCACAAAGCGACTGTGTGCGAGCTGAACGGGCAATGCAGGAAGAGTTCTACCTG
GAACTGAAAGAAGGCTTACTGGAGCCGCTGGCAGTGACGGAACGGCTGGCCATTATCTCG
GTGGTAGGTGATGGTATGCGCACCTTGCGTGGGATCTCGGCGAAATTCTTTGCCGCACTG
GCCCGCGCCAATATCAACATTGTCGCCATTGCTCAGGGATCTTCTGAACGCTCAATCTCT
GTCGTGGTAAATAACGATGATGCGACCACTGGCGTGCGCGTTACTCATCAGATGCTGTTC
AATACCGATCAGGTTATCGAAGTGTTTGTGATTGGCGTCGGTGGCGTTGGCGGTGCGCTG
CTGGAGCAACTGAAGCGTCAGCAAAGCTGGCTGAAGAATAAACATATCGACTTACGTGTC
TGCGGTGTTGCCAACTCGAAGGCTCTGCTCACCAATGTACATGGCCTTAATCTGGAAAAC
TGGCAGGAAGAACTGGCGCAAGCCAAAGAGCCGTTTAATCTCGGGCGCTTAATTCGCCTC
GTGAAAGAATATCATCTGCTGAACCCGGTCATTGTTGACTGCACTTCCAGCCAGGCAGTG
GCGGATCAATATGCCGACTTCCTGCGCGAAGGTTTCCACGTTGTCACGCCGAACAAAAAG
GCCAACACCTCGTCGATGGATTACTACCATCAGTTGCGTTATGCGGCGGAAAAATCGCGG
CGTAAATTCCTCTATGACACCAACGTTGGGGCTGGATTACCGGTTATTGAGAACCTGCAA
AATCTGCTCAATGCAGGTGATGAATTGATGAAGTTCTCCGGCATTCTTTCTGGTTCGCTT
TCTTATATCTTCGGCAAGTTAGACGAAGGCATGAGTTTCTCCGAGGCGACCACGCTGGCG
CGGGAAATGGGTTATACCGAACCGGACCCGCGAGATGATCTTTCTGGTATGGATGTGGCG
CGTAAACTATTGATTCTCGCTCGTGAAACGGGACGTGAACTGGAGCTGGCGGATATTGAA
ATTGAACCTGTGCTGCCCGCAGAGTTTAACGCCGAGGGTGATGTTGCCGCTTTTATGGCG
AATCTGTCACAACTCGACGATCTCTTTGCCGCGCGCGTGGCGAAGGCCCGTGATGAAGGA
AAAGTTTTGCGCTATGTTGGCAATATTGATGAAGATGGCGTCTGCCGCGTGAAGATTGCC
GAAGTGGATGGTAATGATCCGCTGTTCAAAGTGAAAAATGGCGAAAACGCCCTGGCCTTC
TATAGCCACTATTATCAGCCGCTGCCGTTGGTACTGCGCGGATATGGTGCGGGCAATGAC
GTTACAGCTGCCGGTGTCTTTGCTGATCTGCTACGTACCCTCTCATGGAAGTTAGGAGTC
TGA

Protein Properties

Pfam Domain Function:

AA_kinase (PF00696 )
ACT (PF01842 )
Homoserine_dh (PF00742 )
NAD_binding_3 (PF03447 )

Protein Residues:

820

Protein Molecular Weight:

89119

Protein Theoretical pI:

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Bifunctional aspartokinase/homoserine dehydrogenase 1
MRVLKFGGTSVANAERFLRVADILESNARQGQVATVLSAPAKITNHLVAMIEKTISGQDA
LPNISDAERIFAELLTGLAAAQPGFPLAQLKTFVDQEFAQIKHVLHGISLLGQCPDSINA
ALICRGEKMSIAIMAGVLEARGHNVTVIDPVEKLLAVGHYLESTVDIAESTRRIAASRIP
ADHMVLMAGFTAGNEKGELVVLGRNGSDYSAAVLAACLRADCCEIWTDVDGVYTCDPRQV
PDARLLKSMSYQEAMELSYFGAKVLHPRTITPIAQFQIPCLIKNTGNPQAPGTLIGASRD
EDELPVKGISNLNNMAMFSVSGPGMKGMVGMAARVFAAMSRARISVVLITQSSSEYSISF
CVPQSDCVRAERAMQEEFYLELKEGLLEPLAVTERLAIISVVGDGMRTLRGISAKFFAAL
ARANINIVAIAQGSSERSISVVVNNDDATTGVRVTHQMLFNTDQVIEVFVIGVGGVGGAL
LEQLKRQQSWLKNKHIDLRVCGVANSKALLTNVHGLNLENWQEELAQAKEPFNLGRLIRL
VKEYHLLNPVIVDCTSSQAVADQYADFLREGFHVVTPNKKANTSSMDYYHQLRYAAEKSR
RKFLYDTNVGAGLPVIENLQNLLNAGDELMKFSGILSGSLSYIFGKLDEGMSFSEATTLA
REMGYTEPDPRDDLSGMDVARKLLILARETGRELELADIEIEPVLPAEFNAEGDVAAFMA
NLSQLDDLFAARVAKARDEGKVLRYVGNIDEDGVCRVKIAEVDGNDPLFKVKNGENALAF
YSHYYQPLPLVLRGYGAGNDVTAAGVFADLLRTLSWKLGV

References

External Links:

Resource	Link
Uniprot ID:	P00561
Uniprot Name:	AK1H_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	85674276
Ecogene ID:	EG10998
Ecocyc:	EG10998
ColiBase:	b0002
Kegg Gene:	b0002
EchoBASE ID:	EB0991
CCDB:	AK1H_ECOLI
BacMap:	16127996

General Reference:

Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
Cossart, P., Katinka, M., Yaniv, M., Saint Girons, I., Cohen, G. N. (1979). "Construction and expression of a hybrid plasmid containing the Escherichia coli thrA and thrB genes." Mol Gen Genet 175:39-44. Pubmed: 390305
Gardner, J. F. (1982). "Initiation, pausing, and termination of transcription in the threonine operon regulatory region of Escherichia coli." J Biol Chem 257:3896-3904. Pubmed: 6277952
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
Katinka, M., Cossart, P., Sibilli, L., Saint-Girons, I., Chalvignac, M. A., Le Bras, G., Cohen, G. N., Yaniv, M. (1980). "Nucleotide sequence of the thrA gene of Escherichia coli." Proc Natl Acad Sci U S A 77:5730-5733. Pubmed: 7003595
Lynn, S. P., Bauer, C. E., Chapman, K., Gardner, J. F. (1985). "Identification and characterization of mutants affecting transcription termination at the threonine operon attenuator." J Mol Biol 183:529-541. Pubmed: 2410621
Sibilli, L., Le Bras, G., Cossart, P., Chalvignac, M. A., Le Bras, G., Briley, P. A., Cohen, G. N. (1979). "The primary structure of Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I : sequence of cyanogen bromide peptide CB 3." Biochimie 61:733-739. Pubmed: 387092
Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901
Zakin, M. M., Duchange, N., Ferrara, P., Cohen, G. N. (1983). "Nucleotide sequence of the metL gene of Escherichia coli. Its product, the bifunctional aspartokinase ii-homoserine dehydrogenase II, and the bifunctional product of the thrA gene, aspartokinase I-homoserine dehydrogenase I, derive from a common ancestor." J Biol Chem 258:3028-3031. Pubmed: 6298218

Bifunctional aspartokinase/homoserine dehydrogenase 1 (P00561)